The B4GAT1 Knockout HCT 116 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population, engineered to disrupt the B4GAT1 gene in the HCT 116 human colorectal carcinoma cell line. This polyclonal pool provides a genetically heterogeneous loss-of-function model for studying B4GAT1-dependent glycosylation pathways in a defined cancer cell background.
The HCT 116 cell line is a widely used model of colorectal carcinoma, derived from a male patient and characterized by near-diploid karyotype, microsatellite instability (MSI-high), and a KRAS G13D activating mutation. These cells retain epithelial properties and are commonly employed to investigate tumor cell adhesion, migration, and signaling in the context of colorectal cancer progression.
B4GAT1 encodes a glucuronyltransferase that catalyzes the addition of glucuronic acid to terminal galactose residues on N- and O-linked glycans. This modification serves as the priming step for LARGE-dependent extension of matriglycan on ??-dystroglycan, a critical receptor for extracellular matrix ligands. B4GAT1 also contributes to HNK-1 glycan biosynthesis. The enzyme functions within a multi-protein glycosylation complex that includes LARGE, POMGNT1, fukutin, FKRP, and POMT1/2. Upstream regulation of B4GAT1 expression is influenced by TGF-?? signaling, the transcription factor SP1, and the Wnt/??-catenin pathway, linking its activity to pathways frequently dysregulated in cancer.
In HCT 116 colorectal carcinoma cells, disruption of B4GAT1 is expected to impair matriglycan synthesis on ??-dystroglycan, leading to altered cell?Cmatrix interactions. Given that MSI-high colorectal cancers exhibit distinct glycosylation patterns and that KRAS mutations drive invasive behavior, this knockout model enables dissection of how B4GAT1-dependent glycosylation influences tumor cell adhesion, migration, and invasion. The polyclonal nature of the cell population provides a robust system to assess heterogeneous responses and identify phenotypically distinct subpopulations arising from loss of B4GAT1 function.
This product is suited for functional studies of dystroglycan glycosylation in colorectal cancer, including western blotting for glycosylated ??-dystroglycan, lectin blotting, and immunofluorescence detection of matriglycan. It can be used in cell adhesion, migration, and invasion assays to evaluate the role of B4GAT1 in tumor biology. Additionally, these cells serve as a platform for drug screening targeting glycosylation-related disorders and for glycomics profiling by mass spectrometry. Together, these applications support mechanistic and translational research in cancer glycosylation and congenital disorders of glycosylation. For further information, contact Ascent Research.
